E0887
Esterase from rabbit liver
lyophilized powder, ≥30 units/mg protein
Synonyme(s) :
Carboxyl esterase, Carboxylic-ester hydrolase
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-773-7
MDL number:
Specific activity:
≥30 units/mg protein
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lyophilized powder
specific activity
≥30 units/mg protein
mol wt
60 kDa
composition
Protein, ≥85% biuret
storage temp.
−20°C
Quality Level
General description
Esterase belongs to the C-family of carboxylesterases. It is a glycoprotein, mainly present in the endoplasmic reticulum of hepatocytes.
Application
Esterase from rabbit liver has been used in a study to investigate a toxic effect of carbamate insecticides. Esterase from rabbit liver has also been used in a study to investigate the effect of simvastatin on expression and activity of a lipoprotein-associated phospholipase A(2).
Esterase from rabbit liver has been used:
- in comparative biophysical studies with bovine bile-salt-activated lipase in the assays with vinyl acetate, triacylglycerols, p-nitrophenyl esters and serine enzyme inhibitors
- in the catalysis and kinetic profiling studies of peptidic compounds
- in in vitro stability assays of prodrug compounds (BMS-292655 and BMS300043)
- in the hydrolysis of oleuropein aglycone (Ole-AG)
The enzyme from Sigma has been used to study the effect of divalent metal ions on the activity of esterase.
Biochem/physiol Actions
Esterase enzyme catalyzes hydrolysis of carboxylic ester to carboxylate and alcohol in the presence of water. Rabbit liver carboxylesterase catalyzes enantioselective hydrolysis of cineol derivatives.
Esterase enzyme has broad substrate specificity. Esterase from rabbit liver has been used to investigate the toxic effect of carbamate insecticides. Esterase from rabbit liver has also been used for the hydrolysis of simvastatin.
Physical form
Lyophilized powder containing Tris buffer salts
Other Notes
One unit will hydrolyze 1.0 μmole of ethyl butyrate to butyric acid and ethanol per min at pH 8.0 at 25 °C.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Z Qiao et al.
The Journal of international medical research, 37(4), 1029-1037 (2009-09-19)
Lipoprotein-associated phospholipase A(2) (Lp-PLA(2)) contributes to atherosclerotic plaque instability and subsequent sudden coronary death. Statins are associated with decreased stroke risk and may improve stability of atherosclerotic plaques. The present study investigated the effect of simvastatin on expression of Lp-PLA(2)
Anna Sobeková et al.
Acta biologica Hungarica, 60(1), 45-54 (2009-04-22)
The activities of the antioxidant and detoxifying enzymes, superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSHPx), glutathione reductase (GR), glutathione-S-transferase (GST), and the content of thiobarbituric acid reactive substances (TBARS) were determined in the liver and kidney of rabbits after
Hansjörg Schwertz et al.
Journal of cardiovascular pharmacology, 52(2), 151-160 (2008-08-02)
Animal data strongly support a role for inflammation in myocardial ischemia reperfusion injury. Attempts at cardioprotection by immunomodulation (such as with the specific C5 antibody pexelizumab) in humans have been disappointing. We hypothesized that a broader spectrum antiinflammatory agent might
Shijin Zhang et al.
Langmuir : the ACS journal of surfaces and colloids, 36(22), 6261-6267 (2020-05-19)
To explore the potential of step-by-step assembly in the fabrication of biological materials, we designed and synthesized two peptide-based molecules for enzyme-instructed hierarchical assembly. Upon the treatment of alkaline phosphatase, one molecule undergoes enzyme-instructed self-assembly forming uniformed nanofibers. The other
Henri Chahinian et al.
Biochimica et biophysica acta, 1801(11), 1195-1204 (2010-07-27)
To differentiate esterases from lipases at the structure-function level, we have compared the kinetic properties and structural features of sequence-related esterase 1 from rabbit liver (rLE) and bile-salt-activated lipase from bovine pancreas (bBAL). In contrast to rLE, bBAL hydrolyses water-insoluble
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